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Hsp110 is required for spindle length control.
J. Cell Biol. 198, 623-636 (2012)
Publ. Version/Full Text Volltext
DOI
PMC
Systematic affinity purification combined with mass spectrometry analysis of N- and C-tagged cytoplasmic Hsp70/Hsp110 chaperones was used to identify new roles of Hsp70/Hsp110 in the cell. This allowed the mapping of a chaperone-protein network consisting of 1,227 unique interactions between the 9 chaperones and 473 proteins and highlighted roles for Hsp70/Hsp110 in 14 broad biological processes. Using this information, we uncovered an essential role for Hsp110 in spindle assembly and, more specifically, in modulating the activity of the widely conserved kinesin-5 motor Cin8. The role of Hsp110 Sse1 as a nucleotide exchange factor for the Hsp70 chaperones Ssa1/Ssa2 was found to be required for maintaining the proper distribution of kinesin-5 motors within the spindle, which was subsequently required for bipolar spindle assembly in S phase. These data suggest a model whereby the Hsp70-Hsp110 chaperone complex antagonizes Cin8 plus-end motility and prevents premature spindle elongation in S phase.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Anaphase-Promoting Complex; Saccharomyces-Cerevisiae; Budding Yeast; Protein Complexes; Mitotic Spindle; Dna-Replication; Exchange Factor; Hsp70 Family; Chaperone; Cell
ISSN (print) / ISBN
0021-9525
e-ISSN
1540-8140
Journal
Journal of Cell Biology, The
Quellenangaben
Volume: 198,
Issue: 4,
Pages: 623-636
Publisher
Rockefeller University Press
Non-patent literature
Publications
Reviewing status
Peer reviewed